Penicillin-binding protein and bacterial _-lactam antibiotic resistance mechanism.doc

 PAGE \* MERGEFORMAT 17 Penicillin-binding protein and bacterial _-lactam antibiotic resistance mechanism [Paper Keywords] penicillin-binding proteins of Staphylococcus aureus Pseudomonas aeruginosa; the bacterial cell wall of E. coli bacteria site binding [Abstract] β -lactam antibiotics (eg penicillins and cephalosporins, etc.) can be specificity with the target sites on the bacterial cell membrane binding, disrupted cell wall peptidoglycan synthesis which led to cell death. As the target sites with the isotope-labeled penicillin G for covalent binding, so these target sites called penicillin-binding protein (Penicillin binding pro-teins, PBP’s). Some leather-negative bacteria and a few Blue’s Blue’s leather-positive bacteria can produce a variety of β -lactamases, these enzymes can be hydrolyzed antibiotics such as penicillin and cephalosporins, leaving these cells are resistant to β -lactam antibiotics in the ability of anti - . Has proven that β -lactamase-producing plasmid and chromosomal genes. Who do not produce β -lactam of β -amine antibiotics (eg penicillins and Cephalosporins, etc.) can be specificity with the target sites on the bacterial cell membrane binding, disrupted cell wall peptidoglycan synthesis which led to cell death. Because target sites with the isotope-labeled penicillin G for covalent binding, so these target sites called penicillin-binding protein (penieillinbindsng pro-teins, PBP’s). Some leather-negative bacteria and a few Blue’s Blue’s leather-positive bacteria can produce a variety of Thalidomide in β 1 enzyme, these enzymes can be hydrolysis of penicillin and antibiotics such as head hold Abamectin, leaving cells are resistant to these antibiotics, β 1 in Thalidomide killing ability. Has proven that β 1 enzyme within the Thalidomide produces plasmid and chromosomal genes. For the Shonai Thalidomide does not produce the bacterial enzyme in terms of access to a knife a resistance within the Thalidomide’s ability to effect